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Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors.

Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors. Research Abstract Details 

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  • Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors. Abstract Text:

    penny j beuningPenny J Beuning,sharotka m simonSharotka M Simon,veronica g godoyVeronica G Godoy,daniel f jaroszDaniel F Jarosz,graham c walkerGraham C Walker,

    Members of the Y family of DNA polymerases are specialized to replicate lesion-containing DNA. However, they lack 3'-5' exonuclease activity and have reduced fidelity compared to replicative polymerases when copying undamaged templates, and thus are potentially mutagenic. Y family polymerases must be tightly regulated to prevent aberrant mutations on undamaged DNA while permitting replication only under conditions of DNA damage. These polymerases provide a mechanism of DNA damage tolerance, confer cellular resistance to a variety of DNA-damaging agents, and have been implicated in bacterial persistence. The Y family polymerases are represented in all domains of life. Escherichia coli possesses two members of the Y family, DNA pol IV (DinB) and DNA pol V (UmuD'(2)C), and several regulatory factors, including those encoded by the umuD gene that influence the activity of UmuC. This chapter outlines procedures for in vivo and in vitro analysis of these proteins. Study of the E. coli Y family polymerases and their accessory factors is important for understanding the broad principles of DNA damage tolerance and mechanisms of mutagenesis throughout evolution. Furthermore, study of these enzymes and their role in stress-induced mutagenesis may also give insight into a variety of phenomena, including the growing problem of bacterial antibiotic resistance.

    Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors. Publishing Authors By Initials

    pj beuningPJ Beuning,sm simonSM Simon,vg godoyVG Godoy,df jaroszDF Jarosz,gc walkerGC Walker,

    For similar heterocyclic compounds: heterocyclic compounds, 1-ring: pyrimidines: pyrimidinones: uracil: thymine research abstracts see: heterocyclic compounds: heterocyclic compounds, 1-ring: pyrimidines: pyrimidinones: uracil: thymine research

    PUBMED ID PMID:

    MEDLINE DATE:

    Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Methods in enzymology

    VOLUME: 408

    Page Numbers: 318-40

    Journal Abbreviation: Meth. Enzymol.

    ISSN: 0076-6879

    DAY: 3

    MONTH: 12

    YEAR: 2006

    Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 212271

    Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors. Keywords Mesh Terms:

    KEYWORDS: Thymine

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors. Information

    Substance Name: Endopeptidase Clp

    Registry Number: EC 3.4.21.92

    Grant and Affiliation Information for Characterization of Escherichia coli translesion synthesis polymerases and their accessory factors.

    AFFILIATION: Department of Biology, Massachusetts Institute of Technology, Cambridge, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIEHS

    GRANT: P30ES02109

    ACRONYM: ES

    MEDLINETA: Methods Enzymol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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